In:
FEBS Letters, Wiley, Vol. 168, No. 1 ( 1984-03-12), p. 79-83
Abstract:
α 1 ‐Acid glycoprotein (AGP) was purified to homogeneity by a 3‐step procedure using pseudo‐ligand affinity chromatography on immobilized Cibacron blue F3GA, Procion red HE3B, and preparative column isoelectric focusing. The overall yield of the combined techniques was 88%. Analysis of the purified AGP by lectin affinity chromatography on immobilized Con A and immunoaffinoelectrophoresis indicated that the most acidic form did not interact with the lectin, while the two more basic fractions possessed different affinities for Con A. In addition, 3 different populations of AGP were clearly separated by Con A affinity chromatography.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(84)80210-0
Language:
English
Publisher:
Wiley
Publication Date:
1984
detail.hit.zdb_id:
1460391-3
SSG:
12
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